A potent and highly selective sulfotransferase inhibitor

Eli Chapman; Sheng Ding; Peter G. Schultz; Chi Huey Wong

doi:10.1021/ja021086u

A potent and highly selective sulfotransferase inhibitor

Eli Chapman
, Sheng Ding
, Peter G. Schultz
, Chi Huey Wong

Research output: Contribution to journal › Article › peer-review

45 Scopus citations

Abstract

In the present work, we have used a newly developed, fluorescence-based assay to screen a library of >30000 compounds as potential β-arylsulfotransferase-IV inhibitors. A total of 11 inhibitors were discovered. Most of the compounds discovered showed low micromolar inhibition, but one of the compounds showed potent inhibition (K_i = 96 nM). The most potent of these inhibitors was tested against a variety of other purine binding enzymes and showed remarkable specificity.

Original language	English (US)
Pages (from-to)	14524-14525
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	124
Issue number	49
DOIs	https://doi.org/10.1021/ja021086u
State	Published - Dec 11 2002
Externally published	Yes

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja021086u

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abstract = "In the present work, we have used a newly developed, fluorescence-based assay to screen a library of >30000 compounds as potential β-arylsulfotransferase-IV inhibitors. A total of 11 inhibitors were discovered. Most of the compounds discovered showed low micromolar inhibition, but one of the compounds showed potent inhibition (Ki = 96 nM). The most potent of these inhibitors was tested against a variety of other purine binding enzymes and showed remarkable specificity.",

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AU - Wong, Chi Huey

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AB - In the present work, we have used a newly developed, fluorescence-based assay to screen a library of >30000 compounds as potential β-arylsulfotransferase-IV inhibitors. A total of 11 inhibitors were discovered. Most of the compounds discovered showed low micromolar inhibition, but one of the compounds showed potent inhibition (Ki = 96 nM). The most potent of these inhibitors was tested against a variety of other purine binding enzymes and showed remarkable specificity.

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A potent and highly selective sulfotransferase inhibitor

Abstract

ASJC Scopus subject areas

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